DAPD_PSEA7
ID DAPD_PSEA7 Reviewed; 344 AA.
AC A6V1C2;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE EC=2.3.1.117 {ECO:0000255|HAMAP-Rule:MF_02122};
DE AltName: Full=Tetrahydrodipicolinate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE Short=THDP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE Short=THP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE AltName: Full=Tetrahydropicolinate succinylase {ECO:0000255|HAMAP-Rule:MF_02122};
GN Name=dapD {ECO:0000255|HAMAP-Rule:MF_02122}; OrderedLocusNames=PSPA7_1473;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of the cyclic tetrahydrodipicolinate
CC (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using
CC succinyl-CoA. {ECO:0000255|HAMAP-Rule:MF_02122}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-
CC 2-succinylamino-6-oxoheptanedioate + CoA; Xref=Rhea:RHEA:17325,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02122};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC (succinylase route): step 1/3. {ECO:0000255|HAMAP-Rule:MF_02122}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_02122}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02122}.
CC -!- SIMILARITY: Belongs to the type 2 tetrahydrodipicolinate N-
CC succinyltransferase family. {ECO:0000255|HAMAP-Rule:MF_02122}.
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DR EMBL; CP000744; ABR84114.1; -; Genomic_DNA.
DR RefSeq; WP_012074685.1; NC_009656.1.
DR AlphaFoldDB; A6V1C2; -.
DR SMR; A6V1C2; -.
DR EnsemblBacteria; ABR84114; ABR84114; PSPA7_1473.
DR KEGG; pap:PSPA7_1473; -.
DR HOGENOM; CLU_057490_0_0_6; -.
DR OMA; TVLDTWF; -.
DR OrthoDB; 1251912at2; -.
DR UniPathway; UPA00034; UER00019.
DR Proteomes; UP000001582; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008666; F:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.60.70; -; 1.
DR HAMAP; MF_02122; DapD_type2; 1.
DR InterPro; IPR019876; DapD_gammaproteobac.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR032784; THDPS_M.
DR InterPro; IPR038361; THDPS_M_sf.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR InterPro; IPR026586; Type2_DapD.
DR Pfam; PF14602; Hexapep_2; 1.
DR Pfam; PF14789; THDPS_M; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR03536; DapD_gpp; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Diaminopimelate biosynthesis; Lysine biosynthesis; Magnesium;
KW Metal-binding; Transferase.
FT CHAIN 1..344
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase"
FT /id="PRO_0000412265"
FT ACT_SITE 221
FT /note="Acyl-anhydride intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 205
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared between trimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 223
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 238
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 241
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 264
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 279..280
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 287
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 304
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 317..320
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
SQ SEQUENCE 344 AA; 35973 MW; D13F010EA1ABEDBB CRC64;
MSQSLFSLAF GVGTQNRQDA WLEVFYALPL LNPSAEIVAA VAPILGYSSG NQALAFTSQQ
AYQLADALKG IDAAQSALLS RLAESQKPLV ATLLAEDAAP SSTPEAYLKL HLLSHRLVKP
HGVNLSGIFP LLPNVAWTNI GAVDLAELAE LQLEARLKGK LLEVFSVDKF PKMTDYVVPA
GVRIADTARV RLGAYIGEGT TVMHEGFVNF NAGTEGPGMI EGRVSAGVFV GKGSDLGGGC
STMGTLSGGG NIVISVGEGC LIGANAGIGI PLGDRNIVEA GLYITAGTKV ALLDEQNTLV
KVVKARDLAG QPDLLFRRNS QNGAVECKTN KTAIELNEAL HAHN
